This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2y43

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Rad18 ubiquitin ligase RING domain structure

Structural highlights

2y43 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.8Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RAD18_HUMAN E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity.^[1] ^[2]

Publication Abstract from PubMed

The human ubiquitin-conjugating enzyme Rad6 (E2), with ubiquitin ligase enzyme Rad18 (RING E3), monoubiquitinates proliferating cell nuclear antigen at stalled replication forks in DNA translesion synthesis. Here, we determine the structure of the homodimeric Rad18 RING domains by X-ray crystallography and classify it to RING-RING dimers that dimerize through helices adjacent to the RING domains and through the canonical RING domains. Using NMR spectroscopy and site-directed mutagenesis, we demonstrate that the Rad6b binding site, for the Rad18 RING domain, strongly resembles that of other E2/E3 RING/U-box complexes. We show that the homodimeric Rad18 RING domain can recruit two Rad6b E2 enzymes, whereas the full-length Rad18 homodimer binds only to a single Rad6b molecule. Such asymmetry is a common feature of RING-RING heterodimers and has been observed for the CHIP U-box homodimer. We propose that asymmetry may be a common feature of dimeric RING E3 ligases.

Symmetry and Asymmetry of the RING-RING Dimer of Rad18.,Huang A, Hibbert RG, de Jong RN, Das D, Sixma TK, Boelens R J Mol Biol. 2011 Jul 15;410(3):424-35. Epub 2011 Apr 27. PMID:21549715^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Unk I, Hajdu I, Fatyol K, Szakal B, Blastyak A, Bermudez V, Hurwitz J, Prakash L, Prakash S, Haracska L. Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent polyubiquitylation of proliferating cell nuclear antigen. Proc Natl Acad Sci U S A. 2006 Nov 28;103(48):18107-12. Epub 2006 Nov 15. PMID:17108083 doi:0608595103
↑ Cotta-Ramusino C, McDonald ER 3rd, Hurov K, Sowa ME, Harper JW, Elledge SJ. A DNA damage response screen identifies RHINO, a 9-1-1 and TopBP1 interacting protein required for ATR signaling. Science. 2011 Jun 10;332(6035):1313-7. doi: 10.1126/science.1203430. PMID:21659603 doi:10.1126/science.1203430
↑ Huang A, Hibbert RG, de Jong RN, Das D, Sixma TK, Boelens R. Symmetry and Asymmetry of the RING-RING Dimer of Rad18. J Mol Biol. 2011 Jul 15;410(3):424-35. Epub 2011 Apr 27. PMID:21549715 doi:10.1016/j.jmb.2011.04.051

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2y43"

Categories: Homo sapiens | Large Structures | Hibbert RG | Sixma TK

@@ Line 3: / Line 3: @@
 <StructureSection load='2y43' size='340' side='right'caption='[[2y43]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2y43]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y43 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2y43]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Y43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2Y43 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2y43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2y43 OCA], [https://pdbe.org/2y43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2y43 RCSB], [https://www.ebi.ac.uk/pdbsum/2y43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2y43 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/RAD18_HUMAN RAD18_HUMAN]] E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity.<ref>PMID:17108083</ref> <ref>PMID:21659603</ref>
+[https://www.uniprot.org/uniprot/RAD18_HUMAN RAD18_HUMAN] E3 ubiquitin-protein ligase involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. Associates to the E2 ubiquitin conjugating enzyme UBE2B to form the UBE2B-RAD18 ubiquitin ligase complex involved in mono-ubiquitination of DNA-associated PCNA on 'Lys-164'. Has ssDNA binding activity.<ref>PMID:17108083</ref> <ref>PMID:21659603</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 25: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Hibbert, R G]]
+[[Category: Hibbert RG]]
-[[Category: Sixma, T K]]
+[[Category: Sixma TK]]
-[[Category: Dna repair]]
-[[Category: Ligase]]
-[[Category: Metal-binding]]
-[[Category: Translesion synthesis]]
-[[Category: Ubl conjugation pathway]]

2y43

From Proteopedia

Current revision

Rad18 ubiquitin ligase RING domain structure

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox